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Concept explainers
(a)
Interpretation: The validation of the given statement about proteins has to be stated.
Concept introduction: Proteins on hydrolysis are broken down into smaller fragments known as amino acids. They are required by the human body for various biochemical purposes.
(b)
Interpretation: The validation of the given statement about proteins has to be stated.
Concept introduction: Proteins on hydrolysis are broken down into smaller fragments known as amino acids. They are required by the human body for various biochemical purposes.
(c)
Interpretation: The validation of the given statement about proteins has to be stated.
Concept introduction: Proteins on hydrolysis are broken down into smaller fragments known as amino acids. They are required by the human body for various biochemical purposes.
(d)
Interpretation: The validation of the given statement about proteins has to be stated.
Concept introduction: Proteins on hydrolysis are broken down into smaller fragments known as amino acids. They are required by the human body for various biochemical purposes.
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Chapter 20 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- Which of the following statements are correct about the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic interactionsarrow_forwardThe tertiary structure of a protein is established by: a. The sequence of amino acids in the protein b. The molecular weight of the protein c. The total number of amino acids in the protein d. The number of disulfide bridges in the protein e. The net charge of the the protein at physioloical pH.arrow_forwardThe three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are: a. always side by side. b. generally near each other in sequence. c. invariably restricted to about 7 of the 20 standard amino acids. d. often on different polypeptide strands. e. usually near the polypeptide chain's amino terminus or carboxyl terminus.arrow_forward
- Which of the following statements are correct about protein structure (select all that apply)? A. Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein B. Only amino acids with a net charge may interact with other amino acids C. The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role. D. Hydrophobic interactions play a key role in protein folding E. Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acidsarrow_forwardA) List each of the five major functional classes of proteins. B) Discuss the function for each class, give an example of a protein for each class and mention how the function of the protein example fits the function of the class (40 words or less for each class with its examplearrow_forwardWhich of the following statements is FALSE? Select one: a. Secondary structure of a protein determines how it folds up into a unique three dimensional structure. b. Three dimensional structure of a protein determines the function of a protein. c. Primary structure of a protein determines how it folds up into a unique three dimensional structure. d. Amino acid sequence is absolutely important for a particular protein.arrow_forward
- Match the level of protein structure to its description: Primary Secondary Tertiary Quaternary A. Folding due to interactions among the peptide backbone B. Interactions among multiple polypeptide chains C. Sequence of amino acids D. Folding due to interactions among side chainsarrow_forwardWhy do some proteins contain D-amino acids? A. D-amino acids will determine the binding of the protein to its interacting partners. B. D-amino acids will determine whether the structure will be recognized and digested by naturally occurring enzymes C. D-amino acids determines the reactions the proteins will undergo. D. D-amino acids determines the solubility of the protein in aqueous solution. OE. A combination of D and L-amino acids is necessary for the proper folding of protein structures in aqueous solutions.arrow_forwardDescribe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)arrow_forward
- Which of the following statements is true about amino acids? a. All twenty (20) of these protein-derived amino acids are a-amino acids, meaning that the amino group is located on the carbon alpha to the carboxyl group. b. For nineteen (19) of the twenty (20) amino acids, the a-amino group is primary. Glycine is different; its a-amino group is secondary. c. With the exception of proline, the a-carbon of each amino acid is a chiral center. As shown in Table 27.1, all 19 chiral amino acids have the same relative d. Both a & carrow_forwardAt what level of protein structure does each of the following denaturation act? a. heat b. strong acid c. saturated salt solution d. organic solvents (e.g., alcohol or chloroform)arrow_forwardDefine the following terms: a. β-hairpin b. supersecondary structure c. fibrous protein d. globular protein e. mosaic proteinarrow_forward
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